GSTP1_BUFBU
ID GSTP1_BUFBU Reviewed; 210 AA.
AC P81942;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Glutathione S-transferase P 1;
DE EC=2.5.1.18;
DE AltName: Full=BBGSTP1-1;
DE AltName: Full=GST class-pi;
OS Bufo bufo (European toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Bufo.
OX NCBI_TaxID=8384;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Embryo;
RX PubMed=9065793; DOI=10.1042/bj3220679;
RA Sacchetta P., Petruzzelli R., Melino S., Bucciarelli T., Pennelli A.,
RA Amicarelli F., Miranda M., Di Ilio C.;
RT "Amphibian embryo glutathione transferase: amino acid sequence and
RT structural properties.";
RL Biochem. J. 322:679-680(1997).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino
CC acids function as un uncleaved transit peptide, and arginine residues
CC within it are crucial for mitochondrial localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR AlphaFoldDB; P81942; -.
DR SMR; P81942; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Mitochondrion; Nucleus; Transferase.
FT CHAIN 1..210
FT /note="Glutathione S-transferase P 1"
FT /id="PRO_0000185908"
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT DOMAIN 82..203
FT /note="GST C-terminal"
FT BINDING 7
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 44
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 51..52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 64..65
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
SQ SEQUENCE 210 AA; 23820 MW; AC835C0390F3A71D CRC64;
PEYTIIYFNA RGRCEAMRML MADQGAQWKE EVVTSDDWQK GDLKKAAVYG QLPGFKDGDF
TLYQSNAMLR LLARNHDLYG KNPREASLID MVNDGVEDLR LKYLKMIYQN YENGKDDYVK
ALPTNLGHFE RLLASNNEGK GFVVGAHISF ADYNLVDLLH NHLVLAPDCL SGFPLLCAYV
KRISSRPKLE AYLSSDAHKK RPINGNGKQQ
